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Mouse Monoclonal to GCPII / PSMA

GCP-04 (IgG1)

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Glutamate carboxypeptidase II (GCPII), also known as N-acetyl-alpha-linked acidic dipeptidase I (NAALADase I), folate hydrolase (FOLH1), and prostate-specific membrane antigen (PSMA), is an approximately 95-110 kDa type II transmembrane glycoprotein expressed in various tissues. In nervous system GCPII cleaves abundant N-acetylaspartylglutamate, which is released from neurons in a calcium-dependent manner, to N-acetylaspartate and glutamate. As immoderate glutamate concentration is neurotoxic, GCPII contributes to pathological conditions regarding e.g. Alzheimer´s disease, Huntington´s disease, epilepsy, schizophrenia, stroke or neuropathic pain and appears to be an interesting therapeutic target. In jejunum GCPII hydrolyzes pteroylpoly-gamma-glutamate to folate and glutamate, enabling folate to be absorbed by gastrointestinal tract. GCPII, which is present in a number of tissues at low levels, is overexpressed in neovasculature of most solid tumours and is a target enzyme for diagnosis and treatment of prostate cancer. Normal human prostate express more mRNA coding for a cytosolic GCPII form truncated at the N-terminus (PSM´) than mRNA for membrane-bound GCPII, and this ratio is reversed upon malignant transformation.


The antibody GCP-04 recognizes amino acids 100-104 of extracellular domain of denaturated glutamate carboxypeptidase II (PSMA, NAALADase, FOLH1), an approximately 95-110 kDa transmembrane glycoprotein.

Regulatory Status


Recombinant fragment of human GCPII (amino acids 44-750) produced in S2 cells

Species Reactivity:

  • Human
  • Porcine
  • Mouse
  • Rat
  • Other not determined

Negative Species:


  • Western Blotting
    Recommended dilution: 1 μg/ml
    Positive control: LNCaP cell line
    Sample preparation: Resuspend approx. 50 mil. cells in 1 ml cold Lysis buffer (1% NP-40). Incubate 30 min on ice. Mix lysate with non-reducing/reducing Laemmli SDS-PAGE sample buffer.
    Application note: Both reducing and non-reducing conditions.
  • Immunohistochemistry (paraffin sections)
  • Immunocytochemistry
Usage note:
Indicated dilutions are recommended starting points for use of this product. Working concentrations should be determined by the investigator.

General references

  • *Ghadge GD, Slusher BS, Bodner A, Canto MD, Wozniak K, Thomas AG, Rojas C, Tsukamoto T, Majer P, Miller RJ, Monti AL, Roos RP: Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9554-9. [Abstract] [Full Text]
  • *Davis MI, Bennett MJ, Thomas LM, Bjorkman PJ: Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase. Proc. Natl. Acad. Sci. USA 2005, 102: 5981-5986 [Abstract] [Full Text]
  • *Mesters JR, Barinka C, Li W, Tsukamoto T, Majer P, Slusher BS, Konvalinka J, Hilgenfeld R: Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer. EMBO J. 2006, 25: 1375-1384 [Abstract] [Full Text]
  • Product Specific References

  • *Barinka C, Rinnova M, Sacha P, Rojas C, Majer P, Slusher BS, Konvalinka J: Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. J. Neurochem. 2002, 80: 477-487 [Abstract]
  • *Barinka C, Mlcochova P, Sacha P, Hilgert I, Majer P, Slusher BS, Horejsi V, Konvalinka J: Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding. Eur. J. Biochem. 2004, 271: 2782-2790 [Abstract]
  • *Barinka C, Sacha P, Sklenar J, Man P, Bezouska K, Slusher BS, Konvalinka J: Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity. Protein Sci. 2004, 13: 1627-1635 [Abstract] [Full Text]
  • *Sacha P, Zamecnik J, Barinka C, Hlouchova K, Vicha A, Mlcochova P, Hilgert I, Eckschlager T, Konvalinka J: Expression of glutamate carboxypeptidase II in human brain. Neuroscience 2007, 144: 1361-1372 [Abstract]
  • *Rovenska M, Hlouchova K, Sacha P, Mlcochova P, Horak V, Zamecnik J, Barinka C, Konvalinka J: Tissue expression and enzymologic characterization of human prostate specific membrane antigen and its rat and pig orthologs. Prostate 2008, 68: 171-182 [Abstract]
  • *Tykvart J, Navrátil V, Sedlák F, Corey E, Colombatti M, Fracasso G, Koukolík F, Bařinka C, Sácha P, Konvalinka J: Comparative analysis of monoclonal antibodies against prostate-specific membrane antigen (PSMA). Prostate. 2014 Sep 27. doi: 10.1002/pros.22887. [Epub ahead of print] [Abstract]
  • For research use only. Not for drug, diagnostic or other use.

    Related Products

  • Mouse IgG1 Isotype Control
  • Example Data

    PSMA blot
    Fig. 1.

    Fig. 1. Immunostaining of a fragment of human GCPII (aminoacids 44-750) produced in S2 cells on Western blot by GCP-04 monoclonal antibody. Lanes 1, 2, 3 represent 800, 400 and 200 pg of the protein.


    Fig. 2.

    Fig. 2. Immunohistochemistry of GCPII in human Medulla oblongata by GCP-04 monoclonal antibody. Mag. 40x; positive astrocytes in white matter.


    PSMA prostata
    Fig. 3.

    Fig. 3. Immunohistochemistry of GCPII in human prostate by GCP-04 monoclonal antibody. Mag. 400x; positive epithelium of the prostate glands.


    Fig. 4.

    Fig. 4. Immunohistochemistry of GCPII in porcine kidney by GCP-04 monoclonal antibody. Highly positive proximal glomeruli.

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